ENV_SRV2R
ID ENV_SRV2R Reviewed; 574 AA.
AC P51520;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 70;
DE Short=gp70;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 20;
DE Short=gp20;
DE Contains:
DE RecName: Full=R-peptide;
DE Flags: Precursor;
GN Name=env;
OS Simian retrovirus SRV-2 (isolate 2R-18B1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.
OX NCBI_TaxID=73490;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7884914; DOI=10.1128/jvi.69.4.2621-2628.1995;
RA Marracci G.H., Kelley R.D., Pilcher K.Y., Crabtree L., Shiigi S.M.,
RA Avery N., Leo G., Webb M.C., Hallick L.M., Axthelm M.K., Machida A.;
RT "Simian AIDS type D serogroup 2 retrovirus: isolation of an infectious
RT molecular clone and sequence analyses of its envelope glycoprotein gene and
RT 3' long terminal repeat.";
RL J. Virol. 69:2621-2628(1995).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to its receptor. This interaction triggers the refolding of
CC the transmembrane protein (TM) and is thought to activate its fusogenic
CC potential by unmasking its fusion peptide. Fusion occurs at the host
CC cell plasma membrane (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by a labile interchain disulfide bond.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the extravirion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis. {ECO:0000250}.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC N-glycosylated and processed likely by host cell furin or by a furin-
CC like protease in the Golgi to yield the mature SU and TM proteins. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R. The R-peptide is released from the C-terminus of the
CC cytoplasmic tail of the TM protein upon particle formation as a result
CC of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
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DR EMBL; L38695; AAA68002.1; -; Genomic_DNA.
DR SMR; P51520; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..574
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239607"
FT CHAIN 23..382
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040807"
FT CHAIN 383..556
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040808"
FT PEPTIDE 557..574
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239608"
FT TOPO_DOM 23..514
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 386..406
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 446..462
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 407..457
FT /evidence="ECO:0000255"
FT COILED 467..503
FT /evidence="ECO:0000255"
FT MOTIF 243..246
FT /note="CXXC"
FT MOTIF 463..471
FT /note="CX6CC"
FT MOTIF 558..561
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT SITE 382..383
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 556..557
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 243..471
FT /note="Interchain (between SU and TM chains, or C-246 with
FT C-471); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 243..246
FT /evidence="ECO:0000250"
FT DISULFID 463..470
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 63014 MW; 484EAF73ECABD0D6 CRC64;
MTVKDIPFWR VLLIFQTARV YAGFGDPREA ITIIHQQHGK PCDCAGGYVI TAPTVYLATV
SCSSHTAYQP SDSLKWRCVS NPTLANGENI GNCPCQTFKE SVHSSCYTTY QECFFGNKTY
YTAILASNRA PTIGTSNVPT VLGNTHNLLS AGCTGTVGQH ICWNPKAPVH ISDGGGPQDK
AREIAVQKRL EEIHRSLFPE LRYHPLALPK ARGKEKIDAQ TFNLLTATYS LLNKSNPNLA
NECWLCLPSG NPVPLAIPSN DSFLGSNLSC PIIPPLLVQP LEFINLINAS CLYSPSQNNS
FDVDVGLVEF TNCSTTLNIS HSLCAPNSSV FVCGNNKAYT YLPTNWTGTC VLATLLPDID
IVPGDAPVPV PAIDHYLHRA RRAVQFIPLL VGLGITTAVS TGTTGLGYSI TQYTKLSRQL
ISDVQAISST IQDLQDQVDS LAEVVLQNRR GLDLFTAEQG GICLALQEKC CFYANKSGIV
RDKIKALQED LEKRRKEIID NPFWTGLHGL LPYLLPLLRP LLCLLLLITF GPLIFNKIIA
FVKQQMDAIQ AKPIQVHYHR LEQEDNGGVY LRVS
